Capillary affinity electrophoresis using lectins for the analysis of milk oligosaccharide structure and its application to bovine colostrum oligosaccharides

Kazuki Nakajima, Mitsuhiro Kinoshita, Namiko Matsushita, Tadasu Urashima, Minoru Suzuki, Akemi Suzuki, Kazuaki Kakehi

Research output: Contribution to journalArticlepeer-review

37 Citations (Scopus)

Abstract

Animal colostrum and milk contain complex mixtures of oligosaccharides, which have species-specific profiles. Milk oligosaccharides have various types of structure related to the core structures of glycolipids and N- and O-glycans of glycoproteins and provide a good library to examine the binding of oligosaccharides to various lectins. Recently, we reported a capillary affinity electrophoresis (CAE) method for analyzing the interactions between lectins and complex mixtures of N-linked oligosaccharides prepared from serum glycoproteins [K. Nakajima, Y. Oda, M. Kinoshita, K. Kakehi, J. Proteome Res. 2 (2003) 81-88]. The present paper reports the interactions between 24 milk oligosaccharides and six lectins (PA-I, RCA120, SBA, WGA, UEA-I, and AAL) analyzed using CAE. Based on the resulting data, we constructed a library that enables us to determine nonreducing terminal monosaccharides, such as Gal, GalNAc, GlcNAc, and Fuc, and to differentiate Gal- or Fuc-linked isomers, such as lacto-N-tetraose, lacto-N-neotetraose, and lacto-N-fucopentaose II and III. In addition, using the library, we show that a combination of the lectins can characterize the neutral oligosaccharides derived from bovine colostrum.

Original languageEnglish
Pages (from-to)105-114
Number of pages10
JournalAnalytical Biochemistry
Volume348
Issue number1
DOIs
Publication statusPublished - 01-01-2006
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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